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4lvz
From Proteopedia
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| - | + | ==Structure of the THF riboswitch bound to 2,6-diaminopurine== | |
| - | + | <StructureSection load='4lvz' size='340' side='right' caption='[[4lvz]], [[Resolution|resolution]] 1.77Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4lvz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6AP:9H-PURINE-2,6-DIAMINE'>6AP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sd3|3sd3]], [[4lvv|4lvv]], [[4lvw|4lvw]], [[4lvy|4lvy]], [[4lvx|4lvx]], [[4lw0|4lw0]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lvz RCSB], [http://www.ebi.ac.uk/pdbsum/4lvz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The tetrahydrofolate (THF) riboswitch regulates folate transport and metabolism in a number of Firmicutes by cooperatively binding two molecules of THF. To further understand this riboswitch's specificity for THF, binding and regulatory activity of a series of THF analogs and antifolates were examined. Our data reveal that although binding is dominated by the RNA's interactions with the pterin moiety, the para-aminobenzoic acid (pABA) moiety plays a significant role in transcriptional regulation. Further, we find that adenine and several other analogs bind with high affinity by an alternative binding mechanism. Despite a similar affinity to THF, adenine is a poor regulator of transcriptional attenuation. These results demonstrate that binding alone does not determine a compound's effectiveness in regulating the activity of the riboswitch-a complication in current efforts to develop antimicrobials that target these RNAs. | ||
| - | + | A Disconnect between High-Affinity Binding and Efficient Regulation by Antifolates and Purines in the Tetrahydrofolate Riboswitch.,Trausch JJ, Batey RT Chem Biol. 2014 Feb 20;21(2):205-16. doi: 10.1016/j.chembiol.2013.11.012. Epub, 2014 Jan 2. PMID:24388757<ref>PMID:24388757</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Batey, R T | + | == References == |
| - | [[Category: Trausch, J J | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Batey, R T]] | ||
| + | [[Category: Trausch, J J]] | ||
[[Category: 6-diaminopurine]] | [[Category: 6-diaminopurine]] | ||
[[Category: Aptamer]] | [[Category: Aptamer]] | ||
Revision as of 09:46, 25 January 2015
Structure of the THF riboswitch bound to 2,6-diaminopurine
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Categories: Batey, R T | Trausch, J J | 6-diaminopurine | Aptamer | Bacillus subtili | Bacterial | Bacterial protein | Base sequence | Binding site | Calorimetry | Folic acid | Gene expression regulation | Genetic | Guanine | Leucovorin | Ligand | Magnesium | Molecular sequence data | Mrna | Ncrna | Nucleic acid conformation | Nucleotide | Point mutation | Protein binding | Protein structure | Pseudoknot | Regulation | Riboswitch | Rna | S-adenosylmethionine | Secondary | Streptococcus mutan | Terminator region | Tetrahydrofolate | Thermodynamic | Three-way junction | Transcription
